Based on the cutting-edge instruments and specialized expertise, Creative Enzymes has marched to the world-class enzyme service companies. The high-quality services and professional attitude are our advantages over others. We have responded to high demands on transferases, and the services for uridine phosphorylase are guaranteed with accuracy and reliability.

Uridine phosphorylases (UPs, EC 2.4.2.3) are widespread, having been identified in prokaryotes, yeasts, and higher organisms. This enzyme is a member of the pyrimidine nucleoside phosphorylase class and catalyzes the phosphorolytic cleavage of the C-N glycosidic bond of uridine to give ribose-1-phosphate and uracil. The catalytic reaction is reversible and the enzyme may bind metal to keep stability.

Uridine phosphorylases are key enzymes in the pyrimidine salvage pathway in all organisms. The amino acid sequences of UPs are highly conserved among bacteria, human, and mouse. UPs are identified to inactivate certain purine and pyrimidine nucleoside analogs that possess anti-tumor activity. Therefore, the discovery of selective inhibitors for these enzymes could lead to improvement in the therapeutic activity of these nucleoside analogs. The need for potent and specific inhibitors of UP is furthered supported by the modulating effect of UP on the effectiveness of pyrimidine nucleoside analogues such as 5-fluorouracil (5FU) in chemotherapy. However, because of the high treatment concentration of 5FU and the toxic metabolic products, the administration of exogenous uridine should be applied against the side effects. The enzyme is also a target to elucidate the regulation mechanism to support the clinical use of 5FU. It can be seen that the discovery of inhibitors and modifications of the enzyme are the turning points for further studies. To this end, the activity measurement has become the essential assessment for these exploratory steps. Creative Enzymes is professional in enzyme activity measurement, the superior service quality will satisfy all your research demands.

Figure: The crystal structure for the E. coli uridine phosphorylase complexed with 5-fluorouracil ribose-1-phosphate.
Reference: Caradoc-Davies TT et al. J Mol Biol. 2004 337(2): 337-54.

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